Information on EC 5.4.2.8 - phosphomannomutase

New: Word Map on EC 5.4.2.8
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
5.4.2.8
-
RECOMMENDED NAME
GeneOntology No.
phosphomannomutase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate
show the reaction diagram
alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group transfer
-
-
intramolecular, phosphate group
-
isomerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
beta-1,4-D-mannosyl-N-acetyl-D-glucosamine degradation
-
-
Biosynthesis of secondary metabolites
-
-
d-mannose degradation
-
-
Fructose and mannose metabolism
-
-
GDP-mannose biosynthesis
-
-
L-ascorbate biosynthesis I (L-galactose pathway)
-
-
mannan degradation
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-mannose 1,6-phosphomutase
alpha-D-Mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor.
CAS REGISTRY NUMBER
COMMENTARY hide
59536-73-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cultivar Bd21
-
-
Manually annotated by BRENDA team
Cassia corymbosa
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cultivar Betzes
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
OT3
-
-
Manually annotated by BRENDA team
OT3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain DJ77
-
-
Manually annotated by BRENDA team
strain DJ77
-
-
Manually annotated by BRENDA team
gene pgmG
UniProt
Manually annotated by BRENDA team
gene pgmG
UniProt
Manually annotated by BRENDA team
strain KOD1
-
-
Manually annotated by BRENDA team
cultivars DV877 and IE29-1
-
-
Manually annotated by BRENDA team
gene PMM
UniProt
Manually annotated by BRENDA team
gene PMM
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
alpha-phosphomannomutase1 is required for GDP-mannose and dolichol-phosphate-mannose biosynthesis
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-glucose 6-phosphate
2-deoxy-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
2-deoxyribose 1-phosphate
2-deoxyribose 5-phosphate
show the reaction diagram
-
-
-
-
?
3-phospho-D-glyceric acid
?
show the reaction diagram
-
no mutase activity
-
-
?
alpha-D-glucose 1,6-bisphosphate
?
show the reaction diagram
-
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
alpha-D-mannose-1-phosphate
D-mannose-6-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose-1-phosphate
D-fructose-6-phosphate
show the reaction diagram
-
no mutase activity
-
-
?
D-glucosamine-1-phosphate
D-glucosamine-6-phosphate
show the reaction diagram
-
low enzyme activity
-
-
?
D-glucose 1-phosphate
D-glucose 6-phosphate
show the reaction diagram
D-glucose-1-phosphate
D-glucose-6-phosphate
show the reaction diagram
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
D-mannose 6-phosphate
alpha-D-mannose 1-phosphate
show the reaction diagram
D-mannose 6-phosphate
D-mannose 1-phosphate
show the reaction diagram
D-mannose-1-phosphate
D-mannose-6-phosphate
show the reaction diagram
D-mannose-1-phosphate
mannose-6-phosphate
show the reaction diagram
-
-
-
-
r
Glucose 1-phosphate
Glucose 6-phosphate
show the reaction diagram
N-acetyl-D-glucosamine-1-phosphate
N-acetyl-D-glucosamine-6-phosphate
show the reaction diagram
-
no mutase activity
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
P26276
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
D-mannose 6-phosphate
alpha-D-mannose 1-phosphate
show the reaction diagram
Q980S1
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
D-mannose 6-phosphate
D-mannose 1-phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
1% relative activity
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-deoxyglucose 6-phosphate
-
-
Be2+
-
in histidine buffer
Cu2+
-
in Tris buffer, no inhibition in histidine buffer
Disperse Blue 56
-
kinetic studies indicate that it is a parabolic, noncompetitive inhibitor. Reduction of the inhibition in the presence of 0.01% Triton X-100
fructose 1-phosphate
-
-
glucose 1-phosphate
-
substrate inhibition of reverse reaction
glucose 6-phosphate
-
poor, competitive with respect to mannose 6-phosphate
IMP
-
IMP stimulates by more than 100fold the intrinsic glucose-1,6-bisphosphatase activity of recombinant PMM1 while inhibiting its phosphoglucomutase activity
mannose 1-phosphate
Mn2+
-
complete inhibition above 2 mM
serum- and glucocorticoid-regulated kinase
-
Sgk1 decreases the enzymatic activity of PMM2 in the basal state and upon insulin stimulation in intact COS-7 cells
-
vanadate
-
0.05 mM, 50% inhibition
Zn2+
-
in Tris buffer, no inhibition in histidine buffer
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-D-glucose 1,6-diphosphate
alpha-D-Mannose 1,6-diphosphate
D-Glucose 1,6-bisphosphate
D-Mannose 1,6-bisphosphate
-
PMM2 requires a hexose bisphosphate for activity, as potent as glucose 1,6-bisphosphate in activation, half-maximal activation in the presence of 0.01 mM and 0.1 mM at 0.0005 mM and 0.001 mM mannose 1,6-bisphosphate, respectively
histidine
Cassia corymbosa
-
required, maximal activation at 10 mM
Insulin
-
incubation with insulin for 45min led to a more than twofold activation of the enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5
2-deoxyribose-1-phosphate
-
90C
0.0127 - 0.4516
alpha-D-glucose 1-phosphate
0.0056 - 0.68
alpha-D-mannose 1-phosphate
0.0075 - 0.0654
D-glucose 1-phosphate
0.0135 - 3
D-glucose-1-phosphate
0.018 - 1.37
D-mannose 1-phosphate
0.3 - 0.5
D-mannose 6-phosphate
Cassia corymbosa
-
-
0.016 - 3.2
D-mannose-1-phosphate
0.0013 - 0.022
glucose 1-phosphate
0.003 - 0.2
mannose 1-phosphate
0.074
mannose 6-phosphate
-
in presence of glucose 1,6-diphosphate
additional information
additional information
-
KM mannose-1-phosphate isoenzyme PH0923S101A not detectable, 37C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012 - 82.93
alpha-D-glucose 1-phosphate
0.18 - 134.9
alpha-D-mannose 1-phosphate
2.85
D-glucose 1-phosphate
Homo sapiens
O15305, Q92871
isoform alpha-PMM1, pH 6.5, 25C
1.72
D-glucose-1-phosphate
Homo sapiens
O15305, Q92871
isoform alpha-PMM2, pH 6.5, 25C
4.4
D-mannose 1-phosphate
Homo sapiens
O15305, Q92871
isoform alpha-PMM1, pH 6.5, 25C
3.9
D-mannose-1-phosphate
Homo sapiens
O15305, Q92871
isoform alpha-PMM2, pH 6.5, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.35 - 37
alpha-D-mannose 1-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
using alpha-D-mannose 1-phosphate as substrate, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
7
-
10mM Mg2+, 90C
7.1
95% of maximum activity
7.4
-
-
7.8
-
kinetic assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
activity range, inactive above and below
5.5 - 7.6
Cassia corymbosa
-
50% of maximal activity at pH 5.5 and at pH 7.6
7.1
-
80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
kinetic assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24 - 37
-
-
30 - 37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.12
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Cassia corymbosa
-
developing
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27900
calculated from amino acid sequence
29000
-
immunoprecipitation using 9e10 antibody
38000
-
gel filtration
41000
Cassia corymbosa
-
density gradient ultracentrifugation
50000
-
SDS-PAGE
55000
-
gel filtration
58000
Cassia corymbosa
-
gel filtration
60000
-
gel filtration
62000
-
gel filtration
105400
-
native enzyme, non-denaturing PAGE
210000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
tetramer
-
4 * 49850, protein encoded by gene TK1108, calculated
additional information
-
structure analysis of the active phosphoenzyme, the inactive dephosphoenzyme, and the phosphoenzyme in complex with the substrate analog xylose 1-phosphate, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isoform alpha-PMM1 in the open conformation, with and without bound substrate alpha-D-mannose 1-phosphate. Protein consists of two domains, the cap and the core. Substrate phosphate group is at a positively charged site of the cap domain, suggesting that substrate binds first to the cap and then is swept into the active site, thereby facilitating its closure over the core domain
free enzyme and in complex with glucose 1,6-bisphosphate at 2.1 and 2.9 A resolution, resp. Comparison with structure of human enzyme
12-15 mg/ml PMM/PGM solution in 10 mM MOPS, crystals grow by hanging-drop vapor diffusion from 1.4 M sodium/potassium tartrate and 100 mM Na-HEPES, pH 7.5 from drops containing 0.002 ml protein and 0.002 ml of well buffer, crystals diffract to 1.75 A
-
crystal structure of the selenomethionine-substituted PMM/PGM at 2.2 A resolution, crystal structure of S108A mutant at 1.75 A resolution
-
in complex with inhibitor xylose 1-phosphate or slow substrate ribose 1-phosphate. Both ligands induce an interdomain rearrangement, using different enzyme-ligand interactions
-
mutant enzyme P368G, hanging drop vapour diffusion method
-
phospho- and dephospho-enzyme in complex with reaction intermediate glucose 1,6-bisphosphate at 1.9 and 2.0 A
-
purified recombinant detagged enzyme, hanging drop vapor diffusion and microseeding techniques, 1.3 to 1.4 M sodium/potassium tartrate and 100 mM HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
-
purified recombinant detagged enzyme, hanging drop vapour diffusion, from 2 M (NH4)2SO4, 0.2 M NaCl, 0.1 M sodium cacodylate, pH 6.0, 20C, X-ray diffraction structure determination and analysis at 1.86 A resolution, molecular replacement using a modified form of the Leishmania mexicana enzyme, PDB ID 2i54
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
maximal stability
3350
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
-
50% loss of activity within a few min, completely protected from heat inactivation by 1 mM mannose 1-phosphate, 0.01 mM glucose 1,6-diphosphate or 1 mM fructose 1,6-diphosphate. In presence of 1 mM Mg2+: 50% loss of activity after 17 min
50
-
40% loss of activity after 3 min
95
-
longer than 90 min stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
higly unstable during storage
-
Mg2+ stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for at least 2 months
-
0-4C, 50% glycerol, 12 h, 70% loss of activity
-
0-4C, 50% glycerol, 3-4 d, complete loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, Sephadex G-25, KM-cellulose, partially purified
-
cell extracts are purified by His-tag agarose beads
-
heat treatment 85C, 20 min, anion-exchange, hydrophobic and gel filtration column chromatography
-
Ni-NTA column chromatography
-
Ni-Sepharose column chromatography
-
nickel affinity chromatography column chromatography
nickel affinity chromatography column chromatography; nickel affinity chromatography column chromatography; nickel affinity chromatography column chromatography
nickel-affinity column chromatography
-
nickel-chelating resin chromatography
-
partial, alginate-producing strain V388
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3), removal of the His-tag, purification by nickel affinity chromatography and dialysis
-
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration, removal of the His-tag by TEV protease
recombinant PGM
-
recombinant PMM/PGM
-
recombinant PMM2, polyethylene glycol, DEAE-Sepharose, Q-Sepharose
-
Talon metal affinity resin chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells and HEK-293T cells
-
expressed in Escherichia coli strain BL21(DE3)pLysE cells
-
expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli
expressed in Nicotiana tabacum
expressed in Saccharomyces cerevisiae strain BY4741
-
expression in a temperature-sensitive mutant sec53 yeast strain, expression in BHK cells
-
expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression in Escherichia coli with His-tag, expression as green fluorescent protein fusion protein in Arabidospsis thaliana
expression in Leishmania mexicana does not restore virulence of an enzyme deletion mutant
-
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene pgmG, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3), cloning in Escherichia coli strain DH5alpha
gene PMM, DNA and amino acid sequence determination and analysis, expression of His6-tagged enzyme in Escherichia coli
into the vector pET24ma for transformation of Escherichia coli BL21DE3 cells
-
nucleotide sequence of wild-type and mutant algC genes as well as the transcription and translational initiation sites of the wild-type gene
-
overexpression in Escherichia coli
-
overexpression in Escherichia coli BL21
-
overexpression of histidine-tagged fusion protein in Escherichia coli
the vectors pET24ma, pIBR25 and pKC1139 are used
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G7R
-
mutant exhibits activity similar to wild type enzyme
G7R/R37Q
-
temperature-sensitive Arabidopsis thaliana PMM-12 mutant (G7R/R37Q) has lower PMM protein and enzyme activity levels than the wild type enzyme
R37Q
-
mutant exhibits decreased activity similar to wild type enzyme
C241S
the mutant shows 60% residual activity the mutation is associated with phosphomannomutase 2 deficiency
D188G |
mutant of isoform PMM2, 2% of wild-type activiy, involved in congential disorder of glycosylation type 1a
D209G
inactive, the mutation is associated with phosphomannomutase 2 deficiency
E197A
the mutant has wild type activity
F119L
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
F157S
inactive, the mutation is associated with phosphomannomutase 2 deficiency
F207S
inactive, the mutation is associated with phosphomannomutase 2 deficiency
L32R
the mutant shows 45% residual activity the mutation is associated with phosphomannomutase 2 deficiency
P113L
the mutant shows 43% residual activity, the mutation is associated with phosphomannomutase 2 deficiency
P184T
inactive, the mutation is associated with phosphomannomutase 2 deficiency
R123Q
inactive, the mutation is associated with phosphomannomutase 2 deficiency
R162W
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
T118S
the mutant shows 1% residual activity the mutation is associated with phosphomannomutase 2 deficiency
T237M
the mutant shows 48% residual activity the mutation is associated with phosphomannomutase 2 deficiency
V129M
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
V231M
mutant of isoform PMM2, loss of stability at 40C, involved in congential disorder of glycosylation type 1a
V44A
the mutant shows 16% residual activity the mutation is associated with phosphomannomutase 2 deficiency
E325A
-
mutant shows 0.08% of wild type activity
H109Q
-
6% of wild-type activity
H308N
-
100% of wild-type activity
H308N/H329N
-
5% of wild-type activity
H329N
-
6% of wild-type activity
K118L
-
4% of wild-type activity
K118L/H109Q
-
5% of wild-type activity
N110A
-
no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type
P368A
-
mutant shows 10% of wild type activity
P368G
-
mutant shows 8.7% of wild type activity
R15A
-
no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type
R241C
-
0.3% of wild-type acivity, with Km value similar to wild-type
R262A
-
mutant shows 6.1% of wild type activity
R262A/P368G
-
mutant shows 2.5% of wild type activity
S108
-
crystal structure, 5% of wild-type activity
S108A
-
12% of wild-type activity
S108A/H109Q
-
6% of wild-type activity
S108A/H308N
-
3% of wild-type activity
S108A/H329N
-
no activity
S108D
-
7% of wild-type activity
S108V
-
1% of wild-type activity
S10V
-
5% of wild-type activity
S369A
-
mutant shows 20.5% of wild type activity
Y17A
-
mutant shows 0.35% of wild type activity
DELTAmanAB
phosphomannose isomerase, phosphomannosemutase double mutant
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
food industry
medicine
analysis of clinically important mutations involved in congential disorder of glycosylation type 1a; analysis of clinically important mutations involved in congential disorder of glycosylation type 1a
Show AA Sequence (4479 entries)
Please use the Sequence Search for a certain query.